2.350 Å
X-ray
2008-01-30
Name: | Peptidylprolyl isomerase |
---|---|
ID: | Q8I4V8_PLAF7 |
AC: | Q8I4V8 |
Organism: | Plasmodium falciparum |
Reign: | Eukaryota |
TaxID: | 36329 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 60 % |
B | 40 % |
B-Factor: | 27.993 |
---|---|
Number of residues: | 45 |
Including | |
Standard Amino Acids: | 43 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.091 | 1471.500 |
% Hydrophobic | % Polar |
---|---|
45.87 | 54.13 |
According to VolSite |
HET Code: | FK5 |
---|---|
Formula: | C44H69NO12 |
Molecular weight: | 804.018 g/mol |
DrugBank ID: | DB00864 |
Buried Surface Area: | 65.85 % |
Polar Surface area: | 178.36 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 12 |
H-Bond Donors: | 3 |
Rings: | 4 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
0.0537895 | 32.8638 | 15.1557 |
Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand
Ligand | Protein | Interaction | |||
---|---|---|---|---|---|
Atom | Atom | Residue | Distance (Å) | Angle (°) | Type |
C37 | CD1 | LEU- 23 | 3.89 | 0 | Hydrophobic |
C5 | CZ | TYR- 44 | 4 | 0 | Hydrophobic |
C34 | CG2 | VAL- 45 | 4.26 | 0 | Hydrophobic |
C23 | CG2 | VAL- 45 | 4.1 | 0 | Hydrophobic |
C35 | CE1 | PHE- 55 | 4.24 | 0 | Hydrophobic |
O6 | OD2 | ASP- 56 | 2.69 | 157.76 | H-Bond (Ligand Donor) |
C33 | CB | SER- 57 | 3.59 | 0 | Hydrophobic |
C29 | CB | PHE- 59 | 4.15 | 0 | Hydrophobic |
C31 | CB | PHE- 59 | 4.11 | 0 | Hydrophobic |
C33 | CB | PHE- 59 | 4.21 | 0 | Hydrophobic |
C42 | CD1 | PHE- 59 | 3.7 | 0 | Hydrophobic |
C43 | CZ | PHE- 59 | 3.84 | 0 | Hydrophobic |
C17 | CE1 | PHE- 65 | 4.02 | 0 | Hydrophobic |
C36 | CD1 | PHE- 65 | 3.76 | 0 | Hydrophobic |
C41 | CE1 | PHE- 65 | 3.64 | 0 | Hydrophobic |
C4 | CE2 | PHE- 65 | 3.48 | 0 | Hydrophobic |
O10 | O | GLU- 73 | 2.62 | 131.15 | H-Bond (Ligand Donor) |
C3 | CB | VAL- 74 | 4.4 | 0 | Hydrophobic |
C4 | CG1 | VAL- 74 | 4.14 | 0 | Hydrophobic |
C3 | CG1 | ILE- 75 | 4.13 | 0 | Hydrophobic |
C30 | CG2 | ILE- 75 | 4.06 | 0 | Hydrophobic |
O2 | N | ILE- 75 | 3.14 | 150.56 | H-Bond (Protein Donor) |
C5 | CZ2 | TRP- 78 | 3.86 | 0 | Hydrophobic |
C3 | CE2 | TRP- 78 | 3.43 | 0 | Hydrophobic |
C18 | CD | LYS- 90 | 3.97 | 0 | Hydrophobic |
C38 | CD | LYS- 90 | 4.2 | 0 | Hydrophobic |
C30 | CE1 | TYR- 101 | 4.03 | 0 | Hydrophobic |
C35 | CZ | TYR- 101 | 4.28 | 0 | Hydrophobic |
C42 | CE1 | TYR- 101 | 4 | 0 | Hydrophobic |
O3 | OH | TYR- 101 | 2.75 | 174.62 | H-Bond (Protein Donor) |
C12 | SG | CYS- 106 | 4.44 | 0 | Hydrophobic |
C35 | SG | CYS- 106 | 3.94 | 0 | Hydrophobic |
C35 | CD1 | ILE- 110 | 3.61 | 0 | Hydrophobic |
C38 | CB | GLU- 121 | 4.08 | 0 | Hydrophobic |
O10 | O | HOH- 2062 | 2.69 | 179.99 | H-Bond (Protein Donor) |